ID   GLGB1_STRCO             Reviewed;         774 AA.
AC   Q59833; Q9L1K4;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 1;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme 1;
DE   AltName: Full=Glycogen branching enzyme 1;
DE            Short=BE 1;
GN   Name=glgB1; Synonyms=glgBI; OrderedLocusNames=SCO5440;
GN   ORFNames=SC6A11.16c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=8596463; DOI=10.1111/j.1365-2958.1995.mmi_18010089.x;
RA   Bruton C.J., Plaskitt K.A., Chater K.F.;
RT   "Tissue-specific glycogen branching isoenzymes in a multicellular
RT   prokaryote, Streptomyces coelicolor A3(2).";
RL   Mol. Microbiol. 18:89-99(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Schneider D., Bruton C.J., Chater K.F.;
RT   "Duplicated gene clusters reveal a possible 'carbon relay' during aerial
RT   mycelium development in Streptomyces coelicolor A3(2).";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC       in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC       growing alpha-1,4-glucan chains and the subsequent attachment of the
CC       oligosaccharide to the alpha-1,6 position. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC         primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X83397; CAA58314.1; -; Genomic_DNA.
DR   EMBL; AL939123; CAB72416.1; -; Genomic_DNA.
DR   EMBL; AJ001205; CAA04603.1; -; Genomic_DNA.
DR   PIR; S70079; S70079.
DR   RefSeq; NP_629578.1; NC_003888.3.
DR   AlphaFoldDB; Q59833; -.
DR   SMR; Q59833; -.
DR   STRING; 100226.gene:17763092; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 100226-SCO5440; -.
DR   PATRIC; fig|100226.15.peg.5521; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_11; -.
DR   InParanoid; Q59833; -.
DR   OrthoDB; 9800174at2; -.
DR   PhylomeDB; Q59833; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
DR   GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR   CDD; cd11322; AmyAc_Glg_BE; 1.
DR   CDD; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   HAMAP; MF_00685; GlgB; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006407; GlgB.
DR   InterPro; IPR044143; GlgB_N_E_set_prok.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   NCBIfam; TIGR01515; branching_enzym; 1.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF000463; GlgB; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..774
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT                   /id="PRO_0000188749"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        457
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        510
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        146
FT                   /note="T -> R (in Ref. 1; CAA58314/CAA04603)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        766..774
FT                   /note="GTAARRASG -> WHGRPASIRLTLPPLATVWLRPA (in Ref. 1;
FT                   CAA58314)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   774 AA;  85451 MW;  1D55555330F249BF CRC64;
     MTPRPSSSGP DPRKTTGKKP AGKTPTGKKP AKAAKKKAPR RTTASANASA TTSVSGAEVA
     VSPAPDAADR ERLLAGTHHD PHAVLGAHRV PGGVAFRVFR PYALAVTVLS GELRVGLHDD
     GDGFFSGLVP LKDVPAHRLL VAYEGTEQEV EDPYRFLPTL GELDLHLLGE GRHEQLWRAL
     GAHPTTHEGV AGTRFAVWAP NARGVRVAGG FNFWDGTGHP MRSLGSTGVW ELFLPGVGAG
     ELYKFEITRP DGSRTFRADP LARRTEVPPA TSSVVHASDY TWGDEEWLAH RADAPAHEAP
     MSVYEVHLPS WRPGLTYRQL AEQLPAYVAD LGFTHVELMP VAEHPFGGSW GYQVTGFYAP
     TARLGDPDDF KYLVDRLHRA GIGVLMDWVP AHFPRDDWAL AEFDGRPLYE HSDPLRAAHP
     DWGTLEFDFG RREVRNFLVA NAVYWCEEFH IDGLRVDAVA SMLYLDYSRE PGEWEPNEHG
     GRENLDAVAF LQEMNATLYR RVPGVVTVAE ESTAWDGVTR ATHHEGPSGF GGLGFGLKWN
     MGWMHDSLDY MSHEPVHRKH HHGEMTFSMV YAYSENYVLP ISHDEVVHGK RSLVSKMPGD
     WWQQRANERA YLGFMWAHPG KQLLFMGQEF AQGAEWSEAH GPDWWLLDPE YGASADHRGV
     RDLVRDLNTV YRATPALWRR DTHPSGFSWV VGDAAEDNVL AFLRLDADGT PLLAVSNFAP
     VVRSGYRLGV PDEVPAWHEV LNTDAARYGG GDVVNPDPVK PEPQGGTAAR RASG
//